Updated on 2023/03/27

写真a

 
IWADATE Mitsuo
 
Organization
Faculty of Science and Engineering Associate Professor
Other responsible organization
Biological Sciences Course of Graduate School of Science and Engineering, Master's Program
Biological Sciences Course of Graduate School of Science and Engineering, Doctoral Program
External link

Degree

  • 博士(工学) ( 東京農工大学 )

  • 修士(工学) ( 東京農工大学 )

Education

  • 2000.3
     

    Tokyo University of Agriculture and Technology   Graduate School, Division of Engineering   doctor course   completed

  • 1997.3
     

    Tokyo University of Agriculture and Technology   Graduate School, Division of Engineering   master course   completed

  • 1995.3
     

    Tokyo University of Agriculture and Technology   Faculty of Engineering   graduated

  • 1993.3
     

    Oyama National College of Technology   Chemical Engineering Course   graduated

Research History

  • 2011.4 -  

    ~ 日本女子大学理学部・非常勤講師

  • 2002.4 - 2011.3

    理化学研究所ゲノム科学総合センター・客員研究員

  • 2008.4 - 2009.3

    Hokkaido University   School of Science

  • 2008.4 - 2009.3

    Kitasato University   School of Pharmaceutical Sciences

  • 2008.4 -  

    ~ 中央大学理工学部生命科学科・准教授

  • 2003.6 - 2008.3

    Kitasato University   School of Pharmaceutical Sciences

  • 2000.4 - 2003.5

    Kitasato University   School of Pharmaceutical Sciences

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Research Interests

  • 構造生物化学

  • 生物情報学

  • Structured Biochemistry Bioinfomatics

  • ホモロジーモデリング法

  • 核磁気共鳴法

Research Areas

  • Life Science / Structural biochemistry

MISC

  • Method for predicting homology modeling accuracy from amino acid sequence alignment: Power Function

    Iwadate M, Kanou K, Terashi G, Umeyama H, Takeda-Shitaka M

    Chem Pharm Bull   58 ( 1 )   1 - 10   2010.1

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  • HUMAN FAMSD-BASE: High quality protein structure model database for the human genome using the FAMSD homology modeling method

    Kanou K, Hirata H, Iwadate M, Terashi G, Umeyama H, Takeda-Shitaka M

    Chem Pharm Bull   58 ( 1 )   66 - 75   2010.1

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  • Bioinformatics based Ligand-Docking and in-silico screening.

    Takaya D, Takeda-Shitaka M, Terashi G, Kanou K, Iwadate M, Umeyama H

    Chem Pharm Bull   56 ( 5 )   742 - 744   2008.5

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  • fams-ace: A combined method to select the best model after remodeling all server models

    Genki Terashi, Mayuko Takeda-Shitaka, Kazuhiko Kanou, Mitsuo Iwadate, Daisuke Takaya, Akio Hosoi, Kazuhiro Ohta, Hideaki Umeyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   69 ( Suppl8 )   98 - 107   2007

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    Language:English   Publisher:WILEY-LISS  

    During Critical Assessment of Protein Structure Prediction (CASP7, Pacific Grove, CA, 2006), fams-ace was entered in the 3D coordinate prediction category as a human expert group. The procedure can be summarized by the following three steps. (1) All the server models were refined and rebuilt utilizing our homology modeling method. (2) Representative structures were selected from each server, according to a model quality evaluation, based on a 3D1D profile score (like Verify3D). (3) The top five models were selected and submitted in the order of the consensus-based score (like 3D-Jury). Fams-ace is a fully automated server and does not require human intervention. In this article, we introduce the methodology of fams-ace and discuss the successes and failures of this approach during CASP7. In addition, we discuss possible improvements for the next CASP

    DOI: 10.1002/prot.21785

    Web of Science

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  • FAMS-ACE: Model selection from server results using original threading (3D1D) program and consensus

    Mitsuo Iwadate

    CASP7 Abstracts   41 - 42   2006.11

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  • Human FAMSBASE, protein structural model database, with high frequency update

    Mitsuo Iwadate

    20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress Abstracts   4P-B-082   2006.6

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  • RIEKN FAMSBASE

    日本分子生物学会2006フォーラム 分子生物学の未来 要旨集   216   2006

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  • Template based and free modeling in CASP7

    第7回GSICシンポジウム CASP7:タンパク質立体構造予測法の最先端技巧   P.5   2006

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  • FAMS-ACE: Model selection from server results using original threading (3D1D) program and consensus

    CASP7 Abstracts   41 - 42   2006

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  • Human FAMSBASE, protein structural model database, with high frequency update

    20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress Abstracts   4P-B-082   2006

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  • Homology Modeling in CASP6 (Critical Assessment of Techniques for Protein Structure Prediction) Using CHIMERA and FAMS

    Mayuko Takeda-Shitaka

    Genome Informatics Poster Abstracts   138 - 139   2005.12

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  • High Quality Protein Structure Prediction Server, SKE-FAMSD

    Kazuhiko Kanou

    Genome Informatics Poster Abstracts   133 - 134   2005.12

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  • FAMSBASE of Human, Rat and Mouse Genomes with Model Quality Estimation

    Mitsuo Iwadate

    Genome Informatics Poster Abstracts   18 - 19   2005.12

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  • Protein-protein interaction sites predictionand protein-protein docking by the methods of MD, grid scoring and the pair-wise interaction potential in CAPRI Rounds 3-5

    Genki Terashi

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   p.85   2005.8

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  • Fully automated protein structure predictions at CASP6 using homology-modeling server SKE-FAMSD

    Kazuhiko KANOU

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   p.89   2005.8

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  • FAMS Complex: A fully automated homology modeling system for protein comlex structures

    Mayuko TAKEDA-SHITAKA

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   p.88   2005.8

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  • Protein Structure Prediction in the 6th round of Critical Assessment of Technique for Protein Structure Prediction (CASP6) unig CHIMERA and FAMS

    Mayuko TAKEDA-SHITAKA

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   p.86   2005.8

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  • Protein structure prediction in CASP6 using CHIMERA and FAMS

    M Takeda-Shitaka, G Terashi, D Takaya, K Kanou, M Iwadate, H Umeyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   61 ( Suppl 7 )   122 - 127   2005

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    Language:English   Publisher:WILEY-BLACKWELL  

    In CASP6, the CHIMERA-group predicted full-atom models of all targets using SKE-CHIMERA, a Web-user interface system for protein structure prediction that allows human intervention at necessary stages; we used a lot of information from our own data and from publicly available data. Using SKE-CHIMERA, we iterated manual step (template selection and alignment by the in-house program CHIMERA) and automatic step (three-dimensional model building by the in-house program FAMS). The official CASP6 assessment showed that CHIMERA-group was one of the most successful predictors in homology modeling, especially for FR/H (Fold Recognition/Homologous). In this article, we introduce the method of CHIMERA-group and discuss its successes and failures in CASP6.

    DOI: 10.1002/prot.20728

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  • Homology Modeling in CASP6 (Critical Assessment of Techniques for Protein Structure Prediction) Using CHIMERA and FAMS

    Genome Informatics Poster Abstracts   138 - 139   2005

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  • Protein Structure Prediction in the 6th round of Critical Assessment of Technique for Protein Structure Prediction (CASP6) unig CHIMERA and FAMS

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   86   2005

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  • Protein-protein interaction sites predictionand protein-protein docking by the methods of MD, grid scoring and the pair-wise interaction potential in CAPRI Rounds 3-5

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   85   2005

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  • Protein structure prediction in CASP6 using CHIMERA and FAMS

    M Takeda-Shitaka, G Terashi, D Takaya, K Kanou, M Iwadate, H Umeyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   61   122 - 127   2005

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    Language:English   Publisher:WILEY-BLACKWELL  

    In CASP6, the CHIMERA-group predicted full-atom models of all targets using SKE-CHIMERA, a Web-user interface system for protein structure prediction that allows human intervention at necessary stages; we used a lot of information from our own data and from publicly available data. Using SKE-CHIMERA, we iterated manual step (template selection and alignment by the in-house program CHIMERA) and automatic step (three-dimensional model building by the in-house program FAMS). The official CASP6 assessment showed that CHIMERA-group was one of the most successful predictors in homology modeling, especially for FR/H (Fold Recognition/Homologous). In this article, we introduce the method of CHIMERA-group and discuss its successes and failures in CASP6.

    DOI: 10.1002/prot.20728

    Web of Science

    researchmap

  • High Quality Protein Structure Prediction Server, SKE-FAMSD

    Genome Informatics Poster Abstracts   133 - 134   2005

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  • FAMSBASE of Human, Rat and Mouse Genomes with Model Quality Estimation

    Genome Informatics Poster Abstracts   18 - 19   2005

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  • Fully automated protein structure predictions at CASP6 using homology-modeling server SKE-FAMSD

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   89   2005

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  • FAMS Complex: A fully automated homology modeling system for protein comlex structures

    25th ANNIVERSARY INTERNATIONAL CBI CONFERENCE YEAR 2005 PROCEEDINGS   88   2005

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  • Searching protein-protein interaction sites and protein-protein doching with methods of molecular dynamics and grid scoring.

    Hideaki Umeyama

    2nd CAPRI Evaluating Meeting PRELIMINARY PROGRAM   p.30   2004.12

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  • FAMSBASE: Modeling Database of 277 Genomes

    Mitsuo Iwadate

    Genome Informatics Poster Abstracts   159 - 160   2004.12

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  • AUTOMATIC EXTRACTIOPN AND COMPARATIVE PROTEIN MODELING OF ADP/ATP CARRIER PROTEINS AND CA CARRIER/TRANSPORTER PROTEINS FROM ALL THE BIOLOGICAL SPECIES BY FAMS-LIGAND PROGRAM

    Mayuko Takeda-Shitaka

    International Symposium on Calcium in HEALTH and DISEASE BOOK OF ABSTRACTS   2 ( 1 )   69 - 69   2004.7

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  • Normal mode dynamics of the hel-hyhel-10 complex: antigen and antibody interaction is controlled by the constant domains

    H. Umeyama, M. Takeda-Shitaka, M. Iwadate, M. Adachi

    29th FEBS Congress   271 ( 1 )   p.92   2004.7

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  • Evaluation of homology modeling of the severe acute respiratory syndrome (SARS) coronavirus main protease for structure based drug design.

    Takeda-Shitaka

    Chem Pharm Bull (Tokyo)   52 ( 5 )   643 - 5   2004.5

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  • Molecular characterization of ADAMTS13 gene mutations in Japanese patients with Upshaw-Schulman syndrome

    M Matsumoto, K Kokame, K Soejima, M Miura, S Hayashi, Y Fujii, A Iwai, E Ito, Y Tsuji, M Takeda-Shitaka, M Iwadate, H Umeyama, H Yagi, H Ishizashi, F Banno, T Nakagaki, T Miyata, Y Fujimura

    BLOOD   103 ( 4 )   1305 - 1310   2004.2

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    Language:English   Publisher:AMER SOC HEMATOLOGY  

    We report here 7 new mutations in the ADAMTS13 gene responsible for Upshaw-Schulman syndrome (USS), a catastrophic phenotype of congenital thrombotic thrombocytopenic purpura, by analyzing 5 Japanese families. There were 3 mutations that occurred at exon-intron boundaries: 414+1G >A at intron 4, 686+1G >A at intron 6, and 1244+2T>G at intron 10 (numbered from the A of the initiation Met codon), and we confirmed that 2 of these mutations produced aberrantly spliced messenger RNAs (mRNAs). The remainIng 4 mutations were missense mutations: R193W, 1673F, C908Y, and R1123C. In expression experiments using HeLa cells, all mutants showed no or a marginal secretion of ADAMTS13. Taken together with the findings in our recent report we determined the responsible mutations in a total of 7 Japanese patients with USS with a uniform clinical picture of severe neonatal hyperbillrubinemia, and in their family members, based on ADAMTS13 gene analysis. Of these patients, 2 were homozygotes and 5 were compound heterozygotes. The parents of one homozygote were related (cousins), while those of the other were not. Molecular models of the metalloprotease, fifth domain of thrombospondin 1 (Tsp1-5), and Tsp1-8 domains of ADAMTS13 suggest that the missense mutations could cause structural defects in the mutants. (C) 2004 by The American Society of Hematology.

    DOI: 10.1182/blood-2003-06-1796

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  • Molecular characterization of ADAMTS13 gene mutations in Japanese patients with Upshaw-Schulman syndrome

    M Matsumoto, K Kokame, K Soejima, M Miura, S Hayashi, Y Fujii, A Iwai, E Ito, Y Tsuji, M Takeda-Shitaka, M Iwadate, H Umeyama, H Yagi, H Ishizashi, F Banno, T Nakagaki, T Miyata, Y Fujimura

    BLOOD   103 ( 4 )   1305 - 1310   2004.2

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    Language:English   Publisher:AMER SOC HEMATOLOGY  

    We report here 7 new mutations in the ADAMTS13 gene responsible for Upshaw-Schulman syndrome (USS), a catastrophic phenotype of congenital thrombotic thrombocytopenic purpura, by analyzing 5 Japanese families. There were 3 mutations that occurred at exon-intron boundaries: 414+1G >A at intron 4, 686+1G >A at intron 6, and 1244+2T>G at intron 10 (numbered from the A of the initiation Met codon), and we confirmed that 2 of these mutations produced aberrantly spliced messenger RNAs (mRNAs). The remainIng 4 mutations were missense mutations: R193W, 1673F, C908Y, and R1123C. In expression experiments using HeLa cells, all mutants showed no or a marginal secretion of ADAMTS13. Taken together with the findings in our recent report we determined the responsible mutations in a total of 7 Japanese patients with USS with a uniform clinical picture of severe neonatal hyperbillrubinemia, and in their family members, based on ADAMTS13 gene analysis. Of these patients, 2 were homozygotes and 5 were compound heterozygotes. The parents of one homozygote were related (cousins), while those of the other were not. Molecular models of the metalloprotease, fifth domain of thrombospondin 1 (Tsp1-5), and Tsp1-8 domains of ADAMTS13 suggest that the missense mutations could cause structural defects in the mutants. (C) 2004 by The American Society of Hematology.

    DOI: 10.1182/blood-2003-06-1796

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  • FAMS and FAMSBASE for protein structure.

    Umeyama H, Iwadate M

    Curr Protoc Bioinformatics   Chapter 5 ( Unit5.2 )   2004.2

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  • Searching protein-protein interaction sites and protein-protein doching with methods of molecular dynamics and grid scoring.

    2nd CAPRI Evaluating Meeting PRELIMINARY PROGRAM   30   2004

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  • Evaluation of homology modeling of the severe acute respiratory syndrome (SARS) coronavirus main protease for structure based drug design.

    Chem Pharm Bull (Tokyo)   52 ( 5 )   643 - 645   2004

  • Normal mode dynamics of the hel-hyhel-10 complex: antigen and antibody interaction is controlled by the constant domains

    29th FEBS Congress   271 ( 1 )   92   2004

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  • AUTOMATIC EXTRACTIOPN AND COMPARATIVE PROTEIN MODELING OF ADP/ATP CARRIER PROTEINS AND CA CARRIER/TRANSPORTER PROTEINS FROM ALL THE BIOLOGICAL SPECIES BY FAMS-LIGAND PROGRAM

    International Symposium on Calcium in HEALTH and DISEASE BOOK OF ABSTRACTS   2 ( 1 )   69 - 69   2004

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  • FAMSBASE: Modeling Database of 277 Genomes

    Genome Informatics Poster Abstracts   2004

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  • FAMSBASE: Modeling Database of 161 Genomes

    Iwadate Mitsuo, Kanou Kazuhiko, Takaya Daisuke, Komatsu Katsuichiro, Takeda(Shitaka) Mayuko, Umeyama Hideaki

    GI   14 ( 14 )   647 - 648   2003.12

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    Language:English   Publisher:Japanese Society for Bioinformatics  

    DOI: 10.11234/gi1990.14.647

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  • Current Protocols in Bioinformatics

    Hideaki Umeyama, Mitsuo Iwadate, Gregory A, Petsko編

    FAMS and FAMSBASE for Protein Structure   5 ( 2 )   1 - 16   2003.12

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  • FAMS and FAMSBASE: highthroughput Protein Modeling and database

    Hideaki Umeyama, Mistuo Iwadate, Mayuko Takeda-Shitaka

    New Horizons in Molecular Sciences and Systems: An Integrated Approach   p.27   2003.10

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  • Evaluation of the third solvent clusters fitting procedure for the prediction of protein-protein interactions based on the results at the CAPRI blind docking study.

    Komatsu K, Kurihara Y, Iwadate M, Takeda-Shitaka M, Umeyama H

    Proteins.   52 ( 1 )   8 - 15   2003.7

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  • Evaluation of the third solvent clusters fitting procedure for the prediction of protein-protein interactions based on the results at the CAPRI blind docking study

    K Komatsu, Y Kurihara, M Iwadate, M Takeda-Shitaka, H Umeyama

    PROTEINS-STRUCTURE FUNCTION AND GENETICS   52 ( 1 )   15 - 18   2003.7

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    Language:English   Publisher:WILEY-LISS  

    To predict protein-protein interactions, rough or coarse handling for the induced fit problem is proposed. Our method involves the overlap of two hydrophobic interactions as "third solvent clusters fitting." Predictions for binding sites and geometric centers were acceptable, but those of the binding axes were poor. In this study, only the largest benzene cluster was used for the third solvent clusters fitting. For the next CAPRI targets, we must perform protein-protein interaction analyses, which include other smaller benzene clusters. (C) 2003 Wiley-Liss, Inc.

    DOI: 10.1002/prot.10385

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  • Homology Modeling Server for CAFASP3 Contest, advanced FAMS for Proteins

    Hideaki Umeyama, Mistuo Iwadate, Mayuko Takeda-Shitaka

    HGM2003 Poster Abstracts Global Genomics   2003.4

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  • Enlarged FAMSBASE: protein 3D structure models of genome sequences for 41 species

    A Yamaguchi, M Iwadate, E Suzuki, K Yura, S Kawakita, H Umeyama, M Go

    NUCLEIC ACIDS RESEARCH   31 ( 1 )   463 - 468   2003.1

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    Language:English   Publisher:OXFORD UNIV PRESS  

    Enlarged FAMSBASE is a relational database of comparative protein structure models for the whole genome of 41 species, presented in the GTOP database. The models are calculated by Full Automatic Modeling System ( FAMS). Enlarged FAMSBASE provides a wide range of query keys, such as name of ORF ( open reading frame), ORF keywords, Protein Data Bank ( PDB) ID, PDB heterogen atoms and sequence similarity. Heterogen atoms in PDB include cofactors, ligands and other factors that interact with proteins, and are a good starting point for analyzing interactions between proteins and other molecules. The data may also work as a template for drug design. The present number of ORFs with protein 3D models in FAMSBASE is 183 805, and the database includes an average of three models for each ORF. FAMSBASE is available at http: / / famsbase. bio. nagoya- u. ac. jp/ famsbase/

    DOI: 10.1093/nar/gkg117

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  • Enlarged FAMSBASE: protein 3D structure models of genome sequences for 41 species

    A Yamaguchi, M Iwadate, E Suzuki, K Yura, S Kawakita, H Umeyama, M Go

    NUCLEIC ACIDS RESEARCH   31 ( 1 )   463 - 468   2003.1

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    Language:English   Publisher:OXFORD UNIV PRESS  

    Enlarged FAMSBASE is a relational database of comparative protein structure models for the whole genome of 41 species, presented in the GTOP database. The models are calculated by Full Automatic Modeling System ( FAMS). Enlarged FAMSBASE provides a wide range of query keys, such as name of ORF ( open reading frame), ORF keywords, Protein Data Bank ( PDB) ID, PDB heterogen atoms and sequence similarity. Heterogen atoms in PDB include cofactors, ligands and other factors that interact with proteins, and are a good starting point for analyzing interactions between proteins and other molecules. The data may also work as a template for drug design. The present number of ORFs with protein 3D models in FAMSBASE is 183 805, and the database includes an average of three models for each ORF. FAMSBASE is available at http: / / famsbase. bio. nagoya- u. ac. jp/ famsbase/

    DOI: 10.1093/nar/gkg117

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  • FAMS and FAMSBASE: highthroughput Protein Modeling and database

    New Horizons in Molecular Sciences and Systems: An Integrated Approach   27   2003

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  • バイオデータベースとウェブツールの手とり足とり活用法(10頁)

    岩舘満雄, 梅山秀明著, 中村保一, 磯合敦, 石川淳編

    PDB   2 ( 12 )   89 - 98   2003

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  • バイオデータベースとウェブツールの手とり足とり活用法

    岩舘満雄, 梅山秀明著, 中村保一, 磯合敦, 石川淳編

    FAMS   2 ( 13 )   99 - 104   2003

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  • Homology Modeling Server for CAFASP3 Contest, advanced FAMS for Proteins

    HGM2003 Poster Abstracts Global Genomics   Poster 10   2003

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  • ゲノム創薬~合理的創薬からテーラーメード医療実現へ

    岩舘満雄, 梅山秀明著, 田沼靖一編

    タンパク質立体構造のホモロジーモデリング   Ⅰ ( 3 )   39 - 50   2003

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  • Current Protocols in Bioinformatics

    FAMS and FAMSBASE for Protein Structure   5 ( 2 )   1 - 16   2003

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  • FAMSBASE: Modeling Database of 161 Genomes

    Genome Informatics   2003

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  • FAMS and FAMSBASE: Modeling of All the Genomes and Database

    Mitsuo Iwadate, Shigetsugu Kawakita, Hideaki Umeyama

    Genome Informatics   ( 13 )   p.565,p.566   2002.12

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  • 生物物理

    岩舘満雄, 梅山秀明

    日本生物物理学会   42 ( 6 )   2002.12

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  • ホモロジーモデリングの手法開発とゲノム機能推定

    梅山秀明, 岩舘満雄

    ゲノムニュース№4   pp.56-57s   2002.10

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  • Modeling Database of GPCRs using FAMS

    Mitsuo Iwadate, Shigetsugu Kawakita, Hideaki Umeyama

    HGM2002 Poster Abstracts Genome Informatics and Annotation   2002.4

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  • The protein modeling of all the genes and the database

    Hideaki Umeyama, Mistuo Iwadate

    HGM2002 Poster Abstracts Genome Informatics and Annotation   2002.4

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  • Modeling Database of GPCRs using FAMS

    HGM2002 Poster Abstracts Genome Informatics and Annotation   Poster 26   2002

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  • FAMS and FAMSBASE: Modeling of All the Genomes and Database

    Genome Informatics   2002

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  • The protein modeling of all the genes and the database

    HGM2002 Poster Abstracts Genome Informatics and Annotation   Poster 56   2002

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  • TOPICS、CASP4(第4回蛋白質立体構造予測評価広領域会議)に参加して

    岩舘満雄

    ファルマシア   37 ( 8 )   2001.8

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  • Automatic Protein Modeling Method to GPCRs

    Iwadate M

    G Protein-Coupled Receptor   2001.6

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  • Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.

    Iwadate M

    J Biomol NMR   19 ( 2 )   115 - 24   2001.2

  • Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers.

    Hori Y他

    Eur J Biochem.   268 ( 2 )   302 - 9   2001.1

  • Comparative Modeling of CAFASP2 Competition

    Iwadate M, Ebisawa K, Umeyama H

    Chem-Bio Informatics Journal   ( 1 )   136 - 148   2001

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  • ゲノム医科学と基礎からのバイオインフォマティクス

    梅山秀明, 岩舘満雄著

    実験医学増刊   19 ( 11 )   180 - 184   2001

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  • Automatic Protein Modeling Method to GPCRs

    G Protein-Coupled Receptor   2001

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  • Comparative Modeling of CAFASP2 Competition

    Chem-Bio Informatics Journal   ( 1 )   136 - 148   2001

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  • Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers.

    Eur J Biochem.   268 ( 2 )   302 - 309   2001

  • Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.

    J Biomol NMR   19 ( 2 )   115-24.   2001

  • Structure determination of [Arg8]vasopressin methylenedithioether in dimethylsulfoxide using NMR.

    Iwadate M

    Eur J Biochem.   267 ( 14 )   4504 - 10   2000.7

  • Structure determination of [Arg8]vasopressin methylenedithioether in dimethylsulfoxide using NMR.

    Eur J Biochem.   267 ( 14 )   4504 - 4510   2000

  • Solid phase synthesis and biological activities of [Arg8]-vasopressin methylenedithioether.

    Ueki M他

    Bioorg Med Chem Lett.   9 ( 13 )   1767 - 72   1999.7

  • Solid phase synthesis and biological activities of [Arg(8)]-vasopressin methylenedithioether

    M Ueki, T Ikeo, M Iwadate, T Asakura, MP Williamson, J Slaninova

    BIOORGANIC & MEDICINAL CHEMISTRY LETTERS   9 ( 13 )   1767 - 1772   1999.7

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    Language:English   Publisher:PERGAMON-ELSEVIER SCIENCE LTD  

    Solid phase synthesis of [Arg(8)]-vasopressin methylenedithioether, an analog of vasopressin which contains an extra methylene group between the two sulfur atoms of Cys(1) and Cys(6), is described. Methylene insertion occurred easily when the thiol free peptide on a solid support was treated with tetrabutylammonium fluoride in dichloromethane at room temperature for 3 h, The uterotonic in vitro, presser, and antidiuretic activities of the compound were reduced in comparison to [Arg(8)]-vasopressin by one order of magnitude, (C) 1999 Elsevier Science Ltd. All rights reserved.

    DOI: 10.1016/S0960-894X(99)00269-3

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  • C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database.

    Iwadate M, Asakura T, Williamson MP

    J Biomol NMR.   13 ( 3 )   199 - 211   1999.3

  • Structural analysis of silk with 13C NMR chemical shift contour plots.

    Asakura T, Iwadate M, Demura M, Williamson MP

    Int J Biol Macromol.   24 ( 2-3 )   167 - 71   1999.3

  • Structural analysis of silk with 13C NMR chemical shift contour plots.

    Int J Biol Macromol.   24 ( 2/3 )   167 - 171   1999

  • C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database.

    J Biomol NMR.   13 ( 3 )   199 - 211   1999

  • The structure of the melittin tetramer at different temperatures--an NOE-based calculation with chemical shift refinement.

    Iwadate M, Asakura T, Williamson MP

    Eur J Biochem.   257 ( 2 )   479 - 87   1998.10

  • Structure analysis of the melittin tetramer at different temperatures using Chemical Shifts and NOEs

    Mitsuo Iwadate, Tetsuo Asakura, Michael P. Williamson

    International Conferences on Magnetic Resonance in Biological Systems (ICMRBS)   1998.8

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  • Analysis of silk structure using 13C chemical shifts

    Michael P. Williamson, Tetsuo Asakura, Mitsuo Iwadate

    International Symposium on SILK and NMR   1998.8

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  • Structure analysis of the melittin tetramer at different temperatures using Chemical Shifts and NOEs

    International Conferences on Magnetic Resonance in Biological Systems (ICMRBS)   1998

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  • The structure of the melittin tetramer at different temperatures--an NOE-based calculation with chemical shift refinement.

    Eur J Biochem.   257 ( 2 )   479 - 487   1998

  • Analysis of silk structure using 13C chemical shifts

    International Symposium on SILK and NMR   1998

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  • Refinement of the Solution Structure of Neurokinin A (4-10) on the Basis of 1H NMR Chemical Shift Calculations

    T. Asakura

    Peptide Chem.   345 - 348   1996

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  • Refinement of the Solution Structure of Neurokinin A (4-10) on the Basis of 1H NMR Chemical Shift Calculations

    Peptide Chem.   345 - 348   1996

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Presentations

  • 構造予測関数とホモロジーモデリングシステムの構築

    第9回国際バイオEXPO若手研究者発表大会  2010 

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    Presentation type:Poster presentation  

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  • タンパク質構造予測関数とホモロジーモデリングシステムの構築

    第22回バイオ情報学研究発表会  2010 

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  • 2006年CASP7コンテストにおける自動サーバによるタンパク質モデリング:日本、米国、欧州の実力

    第34回構造活性相関シンポジウム要旨集,日本薬学会構造活性相関部会  2006 

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  • RIEKN FAMSBASE

    日本分子生物学会2006フォーラム 分子生物学の未来 要旨集,日本分子生物学会  2006 

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  • Template based and free modeling in CASP7

    第7回GSICシンポジウム CASP7:タンパク質立体構造予測法の最先端技巧,東京工業大学 学術国際除法センター34回分子生物情報研究会  2006 

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  • 277生物種立体構造データベースFAMSBASEと複合体情報を含んだWebインターフェース ASMI Complex

    第7回ワークショップ 微生物ゲノム研究のフロンティア,文部科学省科学研究費特定領域研究「統合ゲノム」  2005 

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  • 3次元構造モデル評価を付加したヒトゲノムタンパク質立体構造データベース

    第8回システムバイオロジー研究会,日本バイオインフォマティクス学会 システムバイオロジー研究会  2005 

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  • ヒト・ラット・マウスの高精度プロテオーム立体構造全自動モデリング・データベース・創薬

    第33回構造活性相関シンポジウム要旨集,日本薬学会構造活性相関部会  2005 

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  • ゲノム中の246生物種の立体構造データベースFAMSBASEとDNAマイクロアレイデータとの融合

    第6回ワークショップ 微生物ゲノム研究のフロンティア,文部科学省科学研究費特定領域研究「統合ゲノム」  2004 

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  • ゲノム規模のタンパク質立体構造モデル構築

    フィジカルファーマフォーラム2004 要旨集,日本薬学会物理系薬学部会  2004 

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  • タンパク質立体構造モデリングツールPDFAMS Pro+

    第一回東北大学バイオサイエンスシンポジウム,東北大学  2004 

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  • タンパク質立体構造モデリングツール PDFAMS Pro+によるモデルの解析

    情報計算化学生物(CBI)学会2004年大会予稿集,情報計算化学生物(CBI)学会  2004 

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  • リガンドを含むタンパク質複合体の全自動モデリング法(FAMS Ligand & Complex)の開発

    第31回構造活性相関シンポジウム要旨集,日本薬学会構造活性相関部会  2003 

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  • Gタンパク結合受容体の立体構造データベースの構築

    文部科学省科学研究費特定領域研究(C)「ゲノム情報科学の新展開」公開シンポジウム 要旨集,ゲノム情報科学領域代表者 高木利久  2002 

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  • 全ゲノム遺伝子タンパク質モデリングとデータベース

    第4回ワークショップ 微生物ゲノム研究のフロンティア,文部科学省科学研究費特定領域研究「統合ゲノム」  2002 

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  • 国際コンテストCASP4に参加して(2):CASP4とCAFASP2におけるComparative ModelingとFold Recognition

    タンパク質高次構造に基づくゲノム情報科学 第一回公開ワークショップ要旨集,文部科学省科学研究費特定領域研究(C)「ゲノム情報科学の新展開」項目D03代表者 郷 通子  2001 

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  • 先端的蛋白質3次元構造モデリング:FAMS for CASP4 & CAFASP2

    2001-1 NMR研究会,高分子学会  2001 

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  • CASP4における北里大グループによるモデリング結果

    第一回日本蛋白質科学会年会 プログラム要旨集,日本蛋白質科学会  2001 

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  • Gタンパク結合受容体のモデリングデータベース

    情報計算化学生物(CBI)学会2001年大会予稿集,情報計算化学生物(CBI)学会  2001 

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  • Gタンパク質結合受容体(GPCR)のモデリングデータベース

    第29回構造活性相関シンポジウム要旨集,日本薬学会医薬化学部会  2001 

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  • ラン藻プロテオームの立体構造データベース:FAMSBASE

    第24回日本分子生物学会年会要旨集,日本分子生物学会年会事務局  2001 

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  • 国際コンテストCASP4、CAFASP2におけるホモロジーモデリング

    第24回日本分子生物学会年会要旨集,日本分子生物学会年会事務局  2001 

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  • 1H NMR化学シフトを用いた生理活性ペプチドの立体構造解析

    高分子年次会,高分子学会  2000 

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  • 自動タンパク質ホモロジーモデリングシステム

    情報計算化学生物(CBI)学会ミレニアムシンポジウム予稿集,情報計算化学生物(CBI)学会  2000 

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  • FAMSBASE:大腸菌および枯草菌の全ORFに対するホモロジー解析と自動モデリング法による蛋白質モデルデータベースの構築

    第28回構造活性相関シンポジウム,日本薬学会医薬化学部会  2000 

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  • 1H NMR化学シフト計算を導入した高圧下でのポリペプチドの構造決定

    高分子年次会,高分子学会  1999 

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  • 固体二次元スピン拡散NMRによる13Cラベル絹フィブロインおよびその化合物の構造解析

    繊維学会年次大会シンポジウム,繊維学会  1998 

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  • タンパク質のNMR化学シフト-構造相関マップを利用した絹の構造解析

    高分子討論会,高分子学会  1998 

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  • NMR化学シフト計算と化学シフトマップに基づくペプチド、タンパク質の構造解析

    NMR討論会,NMR討論会  1998 

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  • ハチ毒ペプチド・メリチンの分子間会合構造の破壊に関する原子座標レベル1H NMR化学シフト計算

    高分子年次会,高分子学会  1997 

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  • 13C NMR化学シフト-立体構造相関の定量化とそれを用いたペプチド、タンパク質の構造決定

    高分子年次会,高分子学会  1997 

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  • 13C NMR化学シフト-立体構造相関の定量化とそのタンパク質遷移の構造決定への応用

    繊維学会年次大会シンポジウム,繊維学会  1997 

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  • 1H および13C NMR化学シフト評価によるペプチド・タンパク質の構造解析

    高分子討論会,高分子学会  1997 

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  • 両親媒性ペプチドの1H NMR構造解析

    高分子討論会,高分子学会  1997 

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  • 両親媒性ペプチドの重水素化SDS中でのNMR構造決定とイオンチャンネル機構の検討

    高分子年次会,高分子学会  1996 

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  • リン脂質膜およびChannelペプチドの配向構造に関する固体・溶液NMR解析

    高分子討論会,高分子学会  1996 

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  • NMR法によるオリゴペプチドホルモン、コレシストキニン類似体の溶液構造の決定

    繊維連合研究発表会,繊維学会  1996 

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  • ガラスプレートを用いた再構成脂質二重層と導入された配向ペプチドの角度依存固体NMR構造解析

    NMR討論会,NMR討論会  1996 

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  • ペプチド・タンパク質の構造解析のためのNMR化学シフト評価法の利用

    NMR討論会,NMR討論会  1996 

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  • ミツバチ毒、メリチンの溶液NMR構造解析

    繊維学会年次大会シンポジウム,繊維学会  1995 

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  • ミツバチ毒、メリチンの水溶液系でのNMR構造解析

    高分子討論会,高分子学会  1995 

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Awards

  • フィジカルファーマフォーラム2004 奨励賞

    2004  

  • CBIポスター賞

    2001  

Research Projects

  • タンパク質を始めとする生体分子の立体構造のその設計に関する研究

    2008 -  

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    Grant type:Competitive

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